Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility.

@article{vale1985, abstract = {Axoplasm from the squid giant axon contains a soluble protein translocator that induces movement of microtubules on glass, latex beads on microtubules, and axoplasmic organelles on microtubules. We now report the partial purification of a protein from squid giant axons and optic lobes that induces these microtubule-based movements and show that there is a homologous protein in bovine brain. The purification of the translocator protein depended primarily on its unusual property of forming a high affinity complex with microtubules in the presence of a nonhydrolyzable ATP analog, adenylyl imidodiphosphate. The protein, once released from microtubules with ATP, migrates on gel filtration columns with an apparent molecular weight of 600 kilodaltons and contains 110-120 and 60-70 kilodalton polypeptides. This protein is distinct in molecular weight and enzymatic behavior from myosin or dynein, which suggests that it belongs to a novel class of force-generating molecules, for which we propose the name kinesin.}, author = {Vale, R. D. and Reese, T. S. and Sheetz, M. P. }, citeulike-article-id = {2948441}, issn = {0092-8674}, journal = {Cell}, keywords = {kinesin}, month = {August}, number = {1}, pages = {39--50}, posted-at = {2008-07-01 15:19:48}, priority = {2}, title = {Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/3926325}, volume = {42}, year = {1985} }

TY - JOUR ID - vale1985 L3 - citeulike-article-id:2948441 N2 - Axoplasm from the squid giant axon contains a soluble protein translocator that induces movement of microtubules on glass, latex beads on microtubules, and axoplasmic organelles on microtubules. We now report the partial purification of a protein from squid giant axons and optic lobes that induces these microtubule-based movements and show that there is a homologous protein in bovine brain. The purification of the translocator protein depended primarily on its unusual property of forming a high affinity complex with microtubules in the presence of a nonhydrolyzable ATP analog, adenylyl imidodiphosphate. The protein, once released from microtubules with ATP, migrates on gel filtration columns with an apparent molecular weight of 600 kilodaltons and contains 110-120 and 60-70 kilodalton polypeptides. This protein is distinct in molecular weight and enzymatic behavior from myosin or dynein, which suggests that it belongs to a novel class of force-generating molecules, for which we propose the name kinesin. IS - 1 JF - Cell SN - 0092-8674 EP - 50 TI - Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility. VL - 42 SP - 39 KW - kinesin AU - Vale, RD AU - Reese, TS AU - Sheetz, MP PY - 1985/08// UR - http://view.ncbi.nlm.nih.gov/pubmed/3926325 ER -